TRY2_ANOGA
ID TRY2_ANOGA Reviewed; 277 AA.
AC P35036; Q5TQD2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Trypsin-2;
DE EC=3.4.21.4;
DE AltName: Full=Antryp2;
DE Flags: Precursor;
GN Name=TRYP2; ORFNames=AGAP008295;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=Suakoko; TISSUE=Midgut;
RX PubMed=8335004; DOI=10.1002/j.1460-2075.1993.tb05951.x;
RA Mueller H.-M., Crampton J.M., della Torre A., Sinden R., Crisanti A.;
RT "Members of a trypsin gene family in Anopheles gambiae are induced in the
RT gut by blood meal.";
RL EMBO J. 12:2891-2900(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Suakoko; TISSUE=Midgut;
RX PubMed=7498434; DOI=10.1006/expr.1995.1128;
RA Mueller H.-M., Catteruccia F., Vizioli J., della Torre A., Crisanti A.;
RT "Constitutive and blood meal-induced trypsin genes in Anopheles gambiae.";
RL Exp. Parasitol. 81:371-385(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Major function may be to aid in digestion of the blood meal.
CC {ECO:0000269|PubMed:8335004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8335004}.
CC -!- TISSUE SPECIFICITY: Midgut. {ECO:0000269|PubMed:8335004}.
CC -!- INDUCTION: By blood meal. {ECO:0000269|PubMed:8335004}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; Z18890; CAA79328.1; -; mRNA.
DR EMBL; Z22930; CAA80518.1; -; Genomic_DNA.
DR EMBL; AAAB01008964; EAL39600.1; -; Genomic_DNA.
DR PIR; S35340; S35340.
DR RefSeq; XP_555167.1; XM_555167.2.
DR AlphaFoldDB; P35036; -.
DR SMR; P35036; -.
DR STRING; 7165.AGAP008295-PA; -.
DR MEROPS; S01.130; -.
DR PaxDb; P35036; -.
DR GeneID; 3291694; -.
DR KEGG; aga:AgaP_AGAP008295; -.
DR CTD; 3291694; -.
DR VEuPathDB; VectorBase:AGAP008295; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P35036; -.
DR OMA; QPPRIDG; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P35036; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Digestion; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..50
FT /note="Activation peptide"
FT /id="PRO_0000028245"
FT CHAIN 51..277
FT /note="Trypsin-2"
FT /id="PRO_0000028246"
FT DOMAIN 51..276
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 91
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 226
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 76..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 201..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 228..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 13
FT /note="V -> L (in Ref. 1; CAA79328 and 2; CAA80518)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="R -> G (in Ref. 1; CAA79328 and 2; CAA80518)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="Y -> F (in Ref. 1; CAA79328 and 2; CAA80518)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> L (in Ref. 1; CAA79328 and 2; CAA80518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 29822 MW; 7C1EAF6FA549B2E7 CRC64;
MSNKIAILLL AVVVAVVACA QAQPSRRHHL VHPLLPRFLP RLHRDSNGHR VVGGFQIDVS
DAPYQVSLQY FNSHRCGGSV LDNKWVLTAA HCTQGLDPSS LAVRLGSSEH ATGGTLVGVL
RTVEHPQYDG NTIDYDFSLM ELETELTFSD AVQPVELPEH EEPVEPGTMA TVSGWGNTQS
AVESSDFLRA ANVPTVSHED CSDAYMWFGE ITDRMLCAGY QQGGKDACQG DSGGPLVADG
KLVGVVSWGY GCAQPGYPGV YGRVASVRDW VRENSGV
